1h2s

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[[Image:1h2s.gif|left|200px]]<br />
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[[Image:1h2s.gif|left|200px]]<br /><applet load="1h2s" size="450" color="white" frame="true" align="right" spinBox="true"
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<applet load="1h2s" size="450" color="white" frame="true" align="right" spinBox="true"
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caption="1h2s, resolution 1.93&Aring;" />
caption="1h2s, resolution 1.93&Aring;" />
'''MOLECULAR BASIS OF TRANSMENBRANE SIGNALLING BY SENSORY RHODOPSIN II-TRANSDUCER COMPLEX'''<br />
'''MOLECULAR BASIS OF TRANSMENBRANE SIGNALLING BY SENSORY RHODOPSIN II-TRANSDUCER COMPLEX'''<br />
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==About this Structure==
==About this Structure==
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1H2S is a [http://en.wikipedia.org/wiki/Protein_complex Protein complex] structure of sequences from [http://en.wikipedia.org/wiki/Natronomonas_pharaonis Natronomonas pharaonis] with BOG and RET as [http://en.wikipedia.org/wiki/ligands ligands]. Structure known Active Site: BOG. Full crystallographic information is available from [http://ispc.weizmann.ac.il/oca-bin/ocashort?id=1H2S OCA].
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1H2S is a [http://en.wikipedia.org/wiki/Protein_complex Protein complex] structure of sequences from [http://en.wikipedia.org/wiki/Natronomonas_pharaonis Natronomonas pharaonis] with BOG and RET as [http://en.wikipedia.org/wiki/ligands ligands]. Known structural/functional Site: <scene name='pdbsite=BOG:Ret Binding Site For Chain A'>BOG</scene>. Full crystallographic information is available from [http://ispc.weizmann.ac.il/oca-bin/ocashort?id=1H2S OCA].
==Reference==
==Reference==
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[[Category: signal transduction]]
[[Category: signal transduction]]
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''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Mon Nov 5 16:26:48 2007''
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''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Tue Dec 18 15:54:27 2007''

Revision as of 13:44, 18 December 2007


1h2s, resolution 1.93Å

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MOLECULAR BASIS OF TRANSMENBRANE SIGNALLING BY SENSORY RHODOPSIN II-TRANSDUCER COMPLEX

Overview

Microbial rhodopsins, which constitute a family of seven-helix membrane, proteins with retinal as a prosthetic group, are distributed throughout, the Bacteria, Archaea and Eukaryota. This family of photoactive proteins, uses a common structural design for two distinct functions: light-driven, ion transport and phototaxis. The sensors activate a signal transduction, chain similar to that of the two-component system of eubacterial, chemotaxis. The link between the photoreceptor and the following, cytoplasmic signal cascade is formed by a transducer molecule that binds, tightly and specifically to its cognate receptor by means of two, transmembrane helices (TM1 and TM2). It is thought that light excitation, of sensory rhodopsin II from Natronobacterium pharaonis (SRII) in complex, with its transducer (HtrII) induces an outward movement of its helix F, (ref. 6), which in turn triggers a rotation of TM2 (ref. 7). It is unclear, how this TM2 transition is converted into a cellular signal. Here we, present the X-ray structure of the complex between N. pharaonis SRII and, the receptor-binding domain of HtrII at 1.94 A resolution, which provides, an atomic picture of the first signal transduction step. Our results, provide evidence for a common mechanism for this process in phototaxis and, chemotaxis.

About this Structure

1H2S is a Protein complex structure of sequences from Natronomonas pharaonis with BOG and RET as ligands. Known structural/functional Site: . Full crystallographic information is available from OCA.

Reference

Molecular basis of transmembrane signalling by sensory rhodopsin II-transducer complex., Gordeliy VI, Labahn J, Moukhametzianov R, Efremov R, Granzin J, Schlesinger R, Buldt G, Savopol T, Scheidig AJ, Klare JP, Engelhard M, Nature. 2002 Oct 3;419(6906):484-7. PMID:12368857

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